"Carbon-Oxygen Lyases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, 
	MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, 
	which enables searching at various levels of specificity.
	
	
		
			
			
				Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.
    
			
			
				
				
					
						| Descriptor ID | 
										
							D019757
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						| MeSH Number(s) | 
						
							 D08.811.520.241 
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						| Concept/Terms | 
						
							
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				Below are MeSH descriptors whose meaning is more general than "Carbon-Oxygen Lyases".
				
			 
			
			
				Below are MeSH descriptors whose meaning is more specific than "Carbon-Oxygen Lyases".
				
			 
		 
	 
 
                                        
                                            
	
	
		
			
			
					
				This graph shows the total number of publications written about "Carbon-Oxygen Lyases" by people in this website by year, and whether "Carbon-Oxygen Lyases" was a major or minor topic of these publications. 
				
					
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				Below are the most recent publications written about "Carbon-Oxygen Lyases" by people in Profiles.
						
					
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Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases. J Mol Biol. 2002 Jan 18; 315(3):373-84.
															
								 
							
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Oxidative DNA damage and 8-hydroxy-2-deoxyguanosine DNA glycosylase/apurinic lyase in human breast cancer. Mol Carcinog. 2001 Aug; 31(4):214-23.
															
								 
							
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A thermostable endonuclease III homolog from the archaeon Pyrobaculum aerophilum. Nucleic Acids Res. 2001 Feb 01; 29(3):604-13.
															
								 
							
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DNA damage recognition and repair pathway coordination revealed by the structural biochemistry of DNA repair enzymes. Prog Nucleic Acid Res Mol Biol. 2001; 68:315-47.
															
								 
							
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Lessons learned from structural results on uracil-DNA glycosylase. Mutat Res. 2000 Aug 30; 460(3-4):183-99.
															
								 
							
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Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3' ends justify the means. Mutat Res. 2000 Aug 30; 460(3-4):211-29.
															
								 
							
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The food of sweet and bitter fancy. Nat Struct Biol. 2000 Jan; 7(1):17-8.
															
								 
							
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Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis. Cell. 1999 Aug 06; 98(3):397-408.
															
								 
							
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Purification and characterization of Thermotoga maritima endonuclease IV, a thermostable apurinic/apyrimidinic endonuclease and 3'-repair diesterase. J Bacteriol. 1999 May; 181(9):2834-9.
															
								 
							
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Envisioning the molecular choreography of DNA base excision repair. Curr Opin Struct Biol. 1999 Feb; 9(1):37-47.